6MPZ

Crystal structure of a double glycine motif protease from AMS/PCAT transporter in complex with the leader peptide

6MPZ の概要

• エントリーDOI: 10.2210/pdb6mpz/pdb
• 分子名称: Double Glycine Motif Protease domain from AMS/PCAT Transporter, peptide aldehyde inhibitor 1 based on the ProcA2.8 leader peptide, 3,6,9,12,15,18-HEXAOXAICOSANE, ... (4 entities in total)
• 機能のキーワード: peptide secretion, peptidase c39 domain, leader peptide, lantibiotic, transport protein
• 由来する生物種: Lachnospiraceae bacterium C6A11; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 72864.67

構造登録者

Dong, S.-H.,Nair, S.K. (登録日: 2018-10-09, 公開日: 2019-02-06, 最終更新日: 2025-04-02)

主引用文献

Bobeica, S.C.,Dong, S.,Huo, L.,Mazo, N.,McLaughlin, M.I.H.,Jimenez-Oses, G.,Nair, S.K.,van der Donk, W.A.
Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease.
Elife, 8:-, 2019

PubMed Abstract: The secretion of peptides and proteins is essential for survival and ecological adaptation of bacteria. Dual-functional ATP-binding cassette transporters export antimicrobial or quorum signaling peptides in Gram-positive bacteria. Their substrates contain a leader sequence that is excised by an N-terminal peptidase C39 domain at a double Gly motif. We characterized the protease domain (LahT150) of a transporter from a lanthipeptide biosynthetic operon in Lachnospiraceae and demonstrate that this protease can remove the leader peptide from a diverse set of peptides. The 2.0 Å resolution crystal structure of the protease domain in complex with a covalently bound leader peptide demonstrates the basis for substrate recognition across the entire class of such transporters. The structural data also provide a model for understanding the role of leader peptide recognition in the translocation cycle, and the function of degenerate, non-functional C39-like domains (CLD) in substrate recruitment in toxin exporters in Gram-negative bacteria.

PubMed: 30638446
DOI: 10.7554/eLife.42305

実験手法

X-RAY DIFFRACTION (2 Å)